Proteomic analysis of a non-virulent mutant of the phytopathogenic bacterium Erwinia chrysanthemi deficient in osmoregulated periplasmic glucans: change in protein expression is not restricted to the envelope, but affects general metabolism

Microbiology (Reading). 2007 Mar;153(Pt 3):760-767. doi: 10.1099/mic.0.2006/000372-0.

Abstract

Osmoregulated periplasmic glucans (OPGs) are general constituents of the envelope of Gram-negative bacteria. They are required for full virulence of bacterial phytopathogens such as Pseudomonas syringae, Xanthomonas campestris and Erwinia chrysanthemi. E. chrysanthemi is a pectinolytic gamma-proteobacterium that causes soft rot disease on a wide range of plant species. In addition to the loss of virulence, opg mutants exhibit a pleiotropic phenotype that affects motility, bile-salt resistance, exoenzyme secretion, exopolysaccharide synthesis and membrane lipid composition. This is believed to be the first proteomic analysis of an OPG-defective mutant of E. chrysanthemi and it revealed that, in addition to the effects described, catabolic enzyme synthesis was enhanced and there was a greater abundance of some proteins catalysing the folding and degradation of proteins needed for various stress responses. Thus, in the opg mutant strain, loss of virulence was the result of a combination of envelope structure changes and cellular metabolism modifications.

MeSH terms

  • Bacterial Proteins / analysis*
  • Bacterial Proteins / isolation & purification
  • Dickeya chrysanthemi / chemistry*
  • Dickeya chrysanthemi / genetics
  • Dickeya chrysanthemi / metabolism
  • Dickeya chrysanthemi / pathogenicity
  • Electrophoresis, Gel, Two-Dimensional
  • Gene Expression Regulation, Bacterial
  • Glucans / biosynthesis*
  • Glucans / genetics
  • Mass Spectrometry
  • Metabolic Networks and Pathways
  • Molecular Chaperones / biosynthesis
  • Mutation*
  • Peptide Hydrolases / biosynthesis
  • Proteome / analysis*
  • Proteome / isolation & purification
  • Proteomics
  • Virulence / genetics

Substances

  • Bacterial Proteins
  • Glucans
  • Molecular Chaperones
  • Proteome
  • Peptide Hydrolases